ID A0A398BIH9_9BACI Unreviewed; 358 AA.
AC A0A398BIH9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Nitric oxide synthase oxygenase {ECO:0000256|ARBA:ARBA00018859, ECO:0000256|PIRNR:PIRNR037219};
DE EC=1.14.14.47 {ECO:0000256|ARBA:ARBA00012735, ECO:0000256|PIRNR:PIRNR037219};
GN ORFNames=D1970_04860 {ECO:0000313|EMBL:RID87540.1};
OS Mesobacillus zeae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1917180 {ECO:0000313|EMBL:RID87540.1, ECO:0000313|Proteomes:UP000265816};
RN [1] {ECO:0000313|EMBL:RID87540.1, ECO:0000313|Proteomes:UP000265816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-247 {ECO:0000313|EMBL:RID87540.1,
RC ECO:0000313|Proteomes:UP000265816};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the production of nitric oxide.
CC {ECO:0000256|ARBA:ARBA00002642, ECO:0000256|PIRNR:PIRNR037219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-arginine + 4 O2 + 3 reduced [flavodoxin] = 5 H(+) + 4 H2O
CC + 2 L-citrulline + 2 nitric oxide + 3 oxidized [flavodoxin];
CC Xref=Rhea:RHEA:52324, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57743, ChEBI:CHEBI:58210; EC=1.14.14.47;
CC Evidence={ECO:0000256|ARBA:ARBA00000737};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR037219, ECO:0000256|PIRSR:PIRSR037219-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037219}.
CC -!- MISCELLANEOUS: This protein is similar to the oxygenase domain of
CC eukaryotic nitric oxide synthases but lacks the reductase domain which,
CC in eukaryotes, is responsible for transfer of electrons to the ferric
CC heme during nitric oxide synthesis. {ECO:0000256|PIRNR:PIRNR037219}.
CC -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC subfamily. {ECO:0000256|ARBA:ARBA00005411,
CC ECO:0000256|PIRNR:PIRNR037219}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RID87540.1}.
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DR EMBL; QWVT01000009; RID87540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398BIH9; -.
DR OrthoDB; 3398374at2; -.
DR Proteomes; UP000265816; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:InterPro.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR CDD; cd00575; NOS_oxygenase; 1.
DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR InterPro; IPR017142; Nitric_oxide_synthase_Oase-su.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR PIRSF; PIRSF037219; NOS_oxygenase; 1.
DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR PROSITE; PS60001; NOS; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR037219};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR037219};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037219};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037219};
KW Reference proteome {ECO:0000313|Proteomes:UP000265816}.
FT DOMAIN 61..68
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|PROSITE:PS60001"
FT BINDING 62
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037219-1"
SQ SEQUENCE 358 AA; 41842 MW; 0E2819CB7FCF0D60 CRC64;
MILNEAEKFI RTAYYELNKT EDEAEQRIAE IRNEISESGS YHHTFEELEH GARMAWRNSN
RCIGRLFWES LTVFDQRNLS REEDIRDAVF SHLDYTTNNG KIRPTITVFR QERNDEPTIR
FWNHQIIRYA GYNTENGVLG DPASLELTRA CEELGWKGEG TRFDVLPLVI QIGSEAPKWY
EIPRDLVLEV PLRHPEYEWF AELGLKWYGV PLISDMMLEI GGIQYKAAPF NGWYMGTEIG
ARNLADEFRY NLLPEVAERM GLNMKKSSSL WKDRAIIELN ASVLHSFNED QVTIVDHHTA
ASQFKVFEDR EKEKERKMTG DWTWLIPPVS PAATHIFHKG YDNEMQKPIY LSQPKAYQ
//
